Analytical Data
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Gene name
hupB
- Application
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Alternative Names
hupB；KMT1A；SUV39H；Histone-lysine N-methyltransferase SUV39H1
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9KHS6
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Expression Region
1-90aa
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AA Sequence
MNKSELIDAIAASADLPKAAAGRALDAVIESVTGALKAGDSVVLVGFGTFSVTDRPARIGRNPQTGKTLEIAAAKKPGFKAGKALKEAVN
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Molecular Weight
22.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
HupB, a key protein involved in the packaging of DNA in bacteria, belongs to the HU family of proteins known for their ability to bind DNA and influence its structure and stability. This protein plays a critical role in various cellular processes, such as DNA replication, repair, and transcriptional regulation, which are essential for bacterial growth and survival. Research into HupB has gained momentum due to its potential implications in understanding bacterial pathogenesis, gene regulation, and as a target for new antimicrobial therapies. By elucidating the structural and functional characteristics of HupB through recombinant protein techniques, scientists aim to uncover its precise mechanisms of action and interactions with other cellular molecules. This knowledge could pave the way for innovative approaches to combat bacterial infections, especially in the context of rising antibiotic resistance. The study of HupB not only enhances our understanding of bacterial biology but also contributes to the broader field of molecular genetics and biotechnology, offering insights that may transcend the boundaries of microbial research and have applications in various industries, including pharmaceuticals and synthetic biology. Thus, HupB presents a promising avenue for research and therapeutic development in the ongoing battle against infectious diseases.
